The Structure and Function of Proteins

Proteins are central to all living processes (Figure 11.1). Many proteins are enzymes, the biological catalysts that drive the chemical reactions of the cell; others are structural components, providing scaffolding and support for membranes, filaments, bone, and hair. Some proteins help transport substances; others have a regulatory, communication, or defense function.

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Figure 11.1: Proteins serve a number of biological functions. (a) The light produced by fireflies is the result of a light-producing reaction between luciferin and ATP catalyzed by the enzyme luciferase. (b) The protein fibroin is the major structural component of spider webs. (c) Castor beans contain a highly toxic protein called ricin.
[Part a: Darwin Dale/Science Source. Part b: Rosemary Calvert/Image­state. Part c: Paroli Galperti /© Cuboimages/Photoshot.]

AMINO ACIDS All proteins are polymers composed of amino acids, linked end to end. Twenty common amino acids are found in proteins (Table 11.1). All of these amino acids are similar in structure: each consists of a central carbon atom bonded to an amino group, a hydrogen atom, a carboxyl group, and an R (radical) group that differs for each amino acid (Figure 11.2a). The amino acids in proteins are joined together by peptide bonds (Figure 11.2b) to form polypeptide chains; a protein consists of one or more polypeptide chains. Like nucleic acids, polypeptides have polarity: one end has a free amino group (NH3+) and the other end has a free carboxyl group (COO). Some proteins consist of only a few amino acids, whereas others may have thousands.

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TABLE 11.1 The twenty common amino acids found in most proteins
Amino acid Three-letter abbreviation One-letter abbreviation Amino acid Three-letter abbreviation One-letter abbreviation
Alanine Ala A Leucine Leu L
Arginine Arg R Lysine Lys K
Asparagine Asn N Methionine Met M
Aspartate Asp D Phenylalanine Phe F
Cysteine Cys C Proline Pro P
Glutamate Glu E Serine Ser S
Glutamine Gln Q Threonine Thr T
Glycine Gly G Tyrosine Tyr Y
Histidine His H Tryptophan Trp W
Isoleucine Ile I Valine Val V
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Figure 11.2: The common amino acids that make up proteins have similar structures. (a) Each amino acid consists of a central carbon atom (Cα) attached to (1) an amino group (NH3+); (2) a carboxyl group (COO); (3) a hydrogen atom (H); and (4) a radical group, designated R. (b) Amino acids are joined together by peptide bonds. In a peptide bond (pink shading), the carboxyl group of one amino acid is covalently attached to the amino group of another amino acid.

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PROTEIN STRUCTURE Like that of nucleic acids, the molecular structure of proteins has several levels of organization. The primary structure of a protein is its sequence of amino acids (Figure 11.3a). Through interactions between neighboring amino acids, a polypeptide chain folds and twists into a secondary structure (Figure 11.3b). Two common secondary structures found in proteins are the beta (β) pleated sheet and the alpha (α) helix. Secondary structures interact and fold further to form a tertiary structure (Figure 11.3c), which is the overall, three-dimensional shape of the protein. The secondary and tertiary structures of a protein are ultimately determined by the primary structure—the amino acid sequence—of the protein. Finally, some proteins consist of two or more polypeptide chains that associate to produce a quaternary structure (Figure 11.3d).

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Figure 11.3: Proteins have several levels of structural organization. Atoms are represented in color as follows: blue, nitrogen; white, hydrogen; black, carbon; red, oxygen.

CONCEPTS

Proteins are polymers consisting of amino acids linked by peptide bonds. The amino acid sequence of a protein is its primary structure. This structure folds to create the secondary and tertiary structures; two or more polypeptide chains may associate to create a quaternary structure.

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What determines the secondary and tertiary structures of a protein?

The amino acid sequence (primary structure) of the protein